Reorganization of actin in platelets stimulated by thrombin as measured by the DNase I inhibition assay.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 76 ·No. 12 ·1979-12-00 ·Pages 6376-80

Carlsson L, Markey F, Blikstad I, Persson T, Lindberg U

Abstract

The effect of thrombin stimulation on actin organization in human platelets has been analyzed by using the DNase I inhibition assay, which is selective for unpolymerized and filamentous actin. The results provide biochemical evidence for the suggestion that stimulation leads to rapid polymerization of actin. The measurements also reveal changes in the polymerization state of actin occurring after cell lysis. These changes are influenced by the concentration of free calcium in the extracts.

MeSH Terms

Actins/blood,metabolism,pharmacology Blood Platelets/ultrastructure Calcium/metabolism Cytoskeleton/metabolism Deoxyribonucleases/antagonists & inhibitors Egtazic Acid/pharmacology Humans Kinetics Polymers Protein Binding Thrombin/pharmacology

Chemicals

Actins Polymers Egtazic Acid Deoxyribonucleases Thrombin Calcium

Authors & Affiliations

5 authors, click to expand affiliations / ORCID

Carlsson L

Markey F

Blikstad I

Persson T

Lindberg U

References (29)

29 references, click to expand

The role of the bound nucleotide in the polymerization of actin.
Biochemistry. 1975 Jul 15;14(14):3250-6 PMID: 1148203
Cycling aggregation patterns of cytoplasmic F-actin coordinated with oscillating tension force generation.
Cell Tissue Res. 1976 Jan 27;165(3):327-44 PMID: 942884
ATP binding to a protease-resistant core of actin.
Proc Natl Acad Sci U S A. 1976 Aug;73(8):2742-6 PMID: 134374
Regulation of motility in nonmuscle cells.
J Cell Biol. 1977 Jul;74(1):1-15 PMID: 141454
Physarum action. Observations on its presence, stability, and assembly in plasmodial extracts and development of an improved purification procedure.
Biochemistry. 1977 Nov 1;16(22):4862-71 PMID: 143958
Comparative biochemistry of non-muscle actins.
J Biol Chem. 1977 Nov 25;252(22):8300-9 PMID: 144137
Biochemistry of actomyosin-dependent cell motility (a review).
Proc Natl Acad Sci U S A. 1978 Feb;75(2):588-99 PMID: 147464
Calcium control of enzyme reactions.
Nature. 1978 Nov 16;276(5685):211-2 PMID: 152411
Phosphorylated proteins as physiological effectors.
Science. 1978 Jan 13;199(4325):146-52 PMID: 22932
Association kinetics and binding constants of nucleoside triphosphates with G-actin.
Eur J Biochem. 1977 Apr 1;74(2):227-32 PMID: 404146
Electron microscopical observations on actinoid and myosinoid filaments in blood platelets.
J Ultrastruct Res. 1971 Nov;37(3):351-69 PMID: 4108204
Nucleotide leakage from platelets in artificial media: prevention by albumin and other macromolecules and relation to ADP-induced platelet aggregation.
Scand J Haematol. 1973;11(3):241-8 PMID: 4128871
Factors influencing platelet function: adhesion, release, and aggregation.
Pharmacol Rev. 1970 Jun;22(2):97-187 PMID: 4192958
The blood platelet release reaction.
Scand J Haematol Suppl. 1969;8:3-26 PMID: 4242950
Studies on thrombosthenin a, the actin-like moiety of the contractile protein from blood platelets. I. Isolation, characterization and evidence for two forms of thrombosthenin A.
Biochim Biophys Acta. 1972 Oct 31;278(3):577-84 PMID: 4263860
Cell communication, calcium ion, and cyclic adenosine monophosphate.
Science. 1970 Oct 23;170(3956):404-12 PMID: 4318972
The polymerization of actin: its role in the generation of the acrosomal process of certain echinoderm sperm.
J Cell Biol. 1973 Oct;59(1):109-26 PMID: 4356568
Secretory mechanisms. Behaviour of adenine nucleotides during the platelet release reaction induced by adenosine diphosphate and adrenaline.
Biochem J. 1972 Aug;129(1):67-82 PMID: 4675006
Actin polymerizability is influenced by profilin, a low molecular weight protein in non-muscle cells.
J Mol Biol. 1977 Sep 25;115(3):465-83 PMID: 563468
Fine structural alterations induced in platelets by adenosine diphosphate.
Blood. 1968 May;31(5):604-22 PMID: 5646304
Elemental composition of platelet dense bodies.
Ciba Found Symp. 1975;35:239-59 PMID: 58760
Molecular weight and amino acid composition of deoxyribonuclease I.
Biochemistry. 1967 Jan;6(1):335-42 PMID: 6030331
Human platelets contain profilin, a potential regulator of actin polymerisability.
FEBS Lett. 1978 Apr 1;88(1):75-9 PMID: 639995
Platelet actin: sub-cellular distribution and association with profilin.
FEBS Lett. 1978 Jun 1;90(1):84-8 PMID: 658445
Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I.
Cell. 1978 Nov;15(3):935-43 PMID: 728995
Fibrin-blood platelet interaction in a contracting clot.
Br J Haematol. 1975 Sep;31(1):45-50 PMID: 813758
Shape and cytoplasmic filaments in control and lidocaine-treated human platelets.
Blood. 1977 Jul;50(1):39-53 PMID: 871525
Ca2+-dependent protease in human platelets. Specific cleavage of platelet polypeptides in the presence of added Ca2+.
J Biol Chem. 1977 Aug 25;252(16):5602-5 PMID: 885868
Similarities between platelet contraction and cellular motility during mitosis: role of platelet microtubules in clot retraction.
J Cell Sci. 1976 May;20(3):569-88 PMID: 1270531

Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.76.12.6376

Published

1979-12-00

Pages

6376-80

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC411867

Subset

External Links

PubMed source DOI: 10.1073/pnas.76.12.6376 PMC Full Text View journal details

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Reorganization of actin in platelets stimulated by thrombin as measured by the DNase I inhibition assay.

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